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Nucleotide mammalian

With the aid of cytosine permease, flucytosine reaches the fungal cell where it is converted by cytosine deaminase into 5-fluorouracil [51-21-8]. Cytosine deaminase is not present in the host, which explains the low toxicity of 5-FC. 5-Fluorouracil is then phosphorylated and incorporated into RNA and may also be converted into 5-fluorodeoxyuridine monophosphate, which is a potent and specific inhibitor of thymidylate synthetase. As a result, no more thymidine nucleotides are formed, which in turn leads to a disturbance of the DNA-synthesis. These effects produce an inhibition of the protein synthesis and cell repHcation (1,23,24). 5-Fluorouracil caimot be used as an antimycotic. It is poorly absorbed by the fungus to begin with and is also toxic for mammalian cells. [Pg.256]

Mammalian Cells Unlike microbial cells, mammalian cells do not continue to reproduce forever. Cancerous cells have lost this natural timing that leads to death after a few dozen generations and continue to multiply indefinitely. Hybridoma cells from the fusion of two mammalian lymphoid cells, one cancerous and the other normal, are important for mammalian cell culture. They produce monoclonal antibodies for research, for affinity methods for biological separations, and for analyses used in the diagnosis and treatment of some diseases. However, the frequency of fusion is low. If the unfused cells are not killed, the myelomas 1 overgrow the hybrid cells. The myelomas can be isolated when there is a defect in their production of enzymes involved in nucleotide synthesis. Mammahan cells can produce the necessary enzymes and thus so can the fused cells. When the cells are placed in a medium in which the enzymes are necessaiy for survival, the myelomas will not survive. The unfused normal cells will die because of their limited life span. Thus, after a period of time, the hybridomas will be the only cells left ahve. [Pg.2134]

Participation of nucleotides in NO formation processes in mammalian organisms 97CCC1355. [Pg.225]

Welch, W.J. Feramisco, J.R. (1985). Rapid purification of mammalian 70,000 Dalton stress proteins Affinity of the proteins for nucleotides. Mol. Cell. Biol. 5, 1229-1237. [Pg.461]

Wood RD Nucleotide excision repair in mammalian cells. J Biol Chem 1997 272 23465. [Pg.340]

Figure 37-12. Consensus sequences at splice junctions. The 5 (donor or left) and 3 (acceptor or right) sequences are shown. Also shown is the yeast consensus sequence (UACUAAQ for the branch site. In mammalian cells, this consensus sequence is PyNPyPy-PuAPy, where Py is a pyrimidine, Pu is a purine, and N is any nucleotide. The branch site is located 20-40 nucleotides upstream from the 3 site. Figure 37-12. Consensus sequences at splice junctions. The 5 (donor or left) and 3 (acceptor or right) sequences are shown. Also shown is the yeast consensus sequence (UACUAAQ for the branch site. In mammalian cells, this consensus sequence is PyNPyPy-PuAPy, where Py is a pyrimidine, Pu is a purine, and N is any nucleotide. The branch site is located 20-40 nucleotides upstream from the 3 site.
The terms first, second, and third nucleotide refer to the individual nucleotides of a triplet codon. U, uridine nucleotide C, cytosine nucleotide A, adenine nucleotide G, guanine nucleotide Term, chain terminator codon. AUG, which codes for Met, serves as the initiator codon in mammalian cells and encodes for internal methionines in a protein. (Abbreviations of amino acids are explained in Chapter 3.)... [Pg.359]

Subjecting cells to oxidative stress can result in severe metabolic dysfunctions, including peroxidation of membrane lipids, depletion of nicotinamide nucleotides, rises in intracellular free Ca ions, cytoskeletal disruption and DNA damage. The latter is often measured as formation of single-strand breaks, double-strand breaks or chromosomal aberrations. Indeed, DNA damage has been almost invariably observed in a wide range of mammalian cell types exposed to oxidative stress in a number... [Pg.200]

Elbashir SM, Harborth J, Lendeckel W, Yalcin A, Weber K, Tuschl T (2001) Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells. Nature 411 494-498... [Pg.19]

Mammalian thioredoxin reductases are a family of selenium-containing pyridine nucleotide-disulfide oxidoreductases. These enzymes catalyze NADPH-dependent reduction of the redox protein thioredoxin (Trx), which contains a redox-active disulfide and dithiol group and by itself may function as an efficient cytosolic antioxidant [77]. One of the functions of Trx/ thioredoxin reductase system is the NADPH-catalyzed reduction of protein disulfide [78] ... [Pg.912]

The MTHFRs of Arabidopsis and maize have recently been cloned by genomics-based approaches, based on homology with the enzymes from other organisms.17 Like mammalian MTHFRs, the plant enzymes were found to be homodimers of two-domain subunits that are homologous to the mammalian enzymes throughout both domains. However, when the recombinant plant proteins were expressed in yeast, they were found to differ radically from the mammalian MTHFRs in both their pyridine nucleotide preference and their regulatory properties plant enzymes prefer NADH to NADPH, and they are insensitive to AdoMet.17... [Pg.19]

Mattera, R., Pitts, B. J., Entman, M. L., and Bimbaumer, L. (1985) Guanine nucleotide regulation of a mammalian myocardial muscarinic receptor system. Evidence for homo-and heterotropic cooperativity in ligand binding analyzed by computer-assisted curve fitting. J. Biol. Chem. 260,7410-7421. [Pg.258]

The carbonyl reductases catalyze reduction of aldehydes and ketones by reduced pyridine nucleotides (NADH and/or NADPH). As mentioned earlier, alcohol dehydrogenase can perform this function in the presence of a high ratio of NADH to NAD+. Other enzymes capable of carbonyl reduction include the aldehyde and ketone reductases. The aldehyde and ketone reductases have a ubiquitous species distribution, with the enzymes present in organisms ranging from bacteria to vertebrates. The mammalian carbonyl reductases have been extensively reviewed (101). [Pg.352]


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See also in sourсe #XX -- [ Pg.261 , Pg.286 ]




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